Design and Prediction of the Behavior of Proteins on Solid Surfaces

While x-ray crystallography and NMR approaches have determined many protein structures yielding great insight into the behavior of proteins in solution, there are no solved structures of proteins interacting with a solid surface.  Yet, protein interactions with solid surfaces are critical for formation of hard tissue such as bone or shell, and the design of biomaterials or nanobiotechnology components will require engineering of protein interactions with surfaces.  We have used computational protein structure prediction and design approaches to investigate and control the behavior of proteins on solid surfaces.  In this talk, I will briefly review our predictions of the structure of statherin on hydroxyapatite incorporating solid-state NMR measurements, and then I will discuss recent efforts to affect calcite growth by the addition of computationally designed peptides.  Mutant proteins are compared both by computational analysis and by experimental explorations of the resulting mineral structure by SEM and SAED.  Energetic determinants of peptide interactions in silico largely correspond to morphological observations in vitro, but significant work remains to be able to create custom materials through computationally designed proteins.